ID   TRAP_CLVK               Reviewed;         135 AA.
AC   P14976;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1990, sequence version 1.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=Transcriptional activator protein;
DE            Short=TrAP;
DE   AltName: Full=15.2 kDa protein;
DE   AltName: Full=Protein AC2;
DE   AltName: Full=Protein AL2;
GN   ORFNames=AC2, AL2;
OS   African cassava mosaic virus (isolate West Kenyan 844) (ACMV) (Cassava
OS   latent virus (isolate West Kenyan 844)).
OC   Viruses; Monodnaviria; Shotokuvirae; Cressdnaviricota; Repensiviricetes;
OC   Geplafuvirales; Geminiviridae; Begomovirus.
OX   NCBI_TaxID=10818;
OH   NCBI_TaxID=197394; Hewittia sublobata.
OH   NCBI_TaxID=3996; Jatropha multifida (Coralbush).
OH   NCBI_TaxID=194268; Laportea.
OH   NCBI_TaxID=3983; Manihot esculenta (Cassava) (Jatropha manihot).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Stanley J., Gay M.R.;
RT   "Nucleotide sequence of cassava latent virus DNA.";
RL   Nature 301:260-262(1983).
RN   [2]
RP   FUNCTION.
RX   PubMed=10570213; DOI=10.1073/pnas.96.24.14147;
RA   Voinnet O., Pinto Y.M., Baulcombe D.C.;
RT   "Suppression of gene silencing: a general strategy used by diverse DNA and
RT   RNA viruses of plants.";
RL   Proc. Natl. Acad. Sci. U.S.A. 96:14147-14152(1999).
RN   [3]
RP   FUNCTION, AND INTERACTION WITH NICOTIANA BENTHAMIANA ADK2.
RX   PubMed=15919897; DOI=10.1128/jvi.79.12.7410-7418.2005;
RA   Wang H., Buckley K.J., Yang X., Buchmann R.C., Bisaro D.M.;
RT   "Adenosine kinase inhibition and suppression of RNA silencing by
RT   geminivirus AL2 and L2 proteins.";
RL   J. Virol. 79:7410-7418(2005).
CC   -!- FUNCTION: Strong activator of the late viral genes promoters. Enhances
CC       the expression of the capsid protein and nuclear shuttle protein. Acts
CC       as a suppressor of RNA-mediated gene silencing, also known as post-
CC       transcriptional gene silencing (PTGS), a mechanism of plant viral
CC       defense that limits the accumulation of viral RNAs. Suppresses the host
CC       RNA silencing by inhibiting adenosine kinase 2 (ADK2), a kinase
CC       involved in a general methylation pathway. Also suppresses the host
CC       basal defense by interacting with and inhibiting SNF1 kinase, a key
CC       regulator of cell metabolism implicated in innate antiviral defense.
CC       Determines pathogenicity (By similarity). {ECO:0000250,
CC       ECO:0000269|PubMed:10570213, ECO:0000269|PubMed:15919897}.
CC   -!- SUBUNIT: Monomer. Homodimer. Homooligomer. Self-interaction correlates
CC       with nuclear localization and efficient activation of transcription.
CC       Monomers suppress local silencing by interacting with and inactivating
CC       host adenosine kinase 2 (ADK2) in the cytoplasm. Interacts with and
CC       inhibits host SNF1 kinase. Binds to ssDNA (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Host nucleus {ECO:0000250}. Host cytoplasm
CC       {ECO:0000250}. Note=The phosphorylated form appears to accumulate
CC       almost exclusively in the nucleus, whereas the non-phosphorylated form
CC       is found in both nucleus and cytoplasm. {ECO:0000250}.
CC   -!- DOMAIN: The zinc finger and the transactivation region are involved in
CC       PTGS suppression.
CC   -!- PTM: Phosphorylated. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the geminiviridae transcriptional activator
CC       protein family. {ECO:0000305}.
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DR   EMBL; J02057; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   Proteomes; UP000008452; Genome.
DR   GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0019028; C:viral capsid; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR   InterPro; IPR000942; Gemini_AL2.
DR   Pfam; PF01440; Gemini_AL2; 1.
DR   PRINTS; PR00230; GEMCOATAL2.
PE   1: Evidence at protein level;
KW   Activator; DNA-binding; Host cytoplasm; Host nucleus;
KW   Host-virus interaction; Metal-binding; Phosphoprotein;
KW   Suppressor of RNA silencing; Zinc; Zinc-finger.
FT   CHAIN           1..135
FT                   /note="Transcriptional activator protein"
FT                   /id="PRO_0000222224"
FT   ZN_FING         37..54
FT                   /evidence="ECO:0000250"
FT   REGION          77..117
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          120..135
FT                   /note="Transactivation"
FT                   /evidence="ECO:0000250"
FT   MOTIF           17..32
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   135 AA;  15159 MW;  75D24A8CD6368848 CRC64;
     MQSSSPSQNH STQVPIKVTH RQVKKRAIRR RRVDLVCGCS YYLHINCFNH GFTHRGSHHC
     SSSNEWRVYL GNKQSPVFHN HQAPTTTIPA EPGHHNSPGS IQSQPEEGAG DSQMFSQLPD
     LDNLTASDWS FLKGL